α-Synuclein (67-78) (human) trifluoroace

Biochemical Reagents

< -15℃

The Parkinson's disease-associated protein alpha-synuclein (alpha-syn) is not only expressed in the cytoplasm of neurons, but also secreted in the extracellular space and internalized into glial cells through a lipid raft dependent process. Two distinct cholesterol-binding domains in alpha-synuclein were identified by Fantini and coworkers. The tilted peptide of alpha-synuclein (67-78) bound cholesterol with high affinity and was toxic for cultured astrocytes. A cholesterol recognition consensus motif with lower affinity for cholesterol and devoid of toxicity, is encased in the glycosphingolipid-binding domain (34-45) of alpha-synuclein. The authors propose that the association of alpha-synuclein with lipid rafts involves both the binding of alpha-synuclein (34-45) to glycosphingolipids, and the interaction of alpha-synuclein (67-78) with cholesterol.

Trifluoroacetate